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1  in a distinctive spatial pattern within the protein body.
2 in the endoplasmic reticulum surrounding the protein body.
3 nding and assembly of alpha-zeins within the protein body.
4 s, often reaching to the central area of the protein body.
5 signal peptide sequence for targeting to the protein body.
6 equential manner and deposited in ER-derived protein bodies.
7  stages of zein processing and assembly into protein bodies.
8 of the gluten proteins within the ER to form protein bodies.
9 perm in endoplasmic reticulum membrane-bound protein bodies.
10 and unique functions in the stabilization of protein bodies.
11 cialized organelles in the endosperm, called protein bodies.
12 , and a reduction in the number of prolamine protein bodies.
13 g particles are transported to the prolamine protein bodies.
14 tent with their colocalization in developing protein bodies.
15 (storage proteins) were localized within its protein bodies.
16 usters and associated promyelocytic leukemia protein bodies.
17 eposited in unique, zein-specific ER-derived protein bodies.
18 cumulating-vesicles of pumpkin seeds and the protein bodies accumulated by cereal seeds.
19 entified as a major component of these novel protein bodies and its diversion from normal storage pro
20 a-globulin on the periphery of the prolamine protein bodies and packaging in Golgi-associated dense v
21 zein was colocalized in beta-zein-containing protein bodies and that the level of delta-zein was five
22 d to BS, localizes to promyelocytic leukemia protein bodies and to the nucleolus of the cell, the sit
23 signal peptide sequence for targeting to the protein body and found to be enriched in starch debranch
24 an opaque, starchy phenotype, malformed zein protein bodies, and highly increased levels of binding p
25 dosperm eEF1A co-localizes with actin around protein bodies, and its accumulation is highly correlate
26 entified as speckles, promyelocytic leukemia protein bodies, and nucleoli.
27 distributed throughout the core in wild-type protein bodies, and this distribution is unaffected in f
28 re distinct from PML (promyelocytic leukemia protein) bodies, and it appeared that Daxx was displaced
29                     P granules and other RNA/protein bodies are membrane-less organelles that may ass
30 The spatial organization of zeins within the protein body, as well as interactions between them, sugg
31 ies that zein protein interactions determine protein body assembly.
32 mma-zeins play an important role in prolamin protein body assembly.
33 endoplasmic reticulum (ER)-dependent oil and protein body biogenesis in peroxisome-deficient maturing
34 the 22-kD alpha-zeins by z1CRNAi resulted in protein body budding structures, indicating that a suffi
35 prolamine RNAs are targeted to the prolamine protein bodies by a mechanism based on RNA signal(s), a
36 ase (RubisCO) is sequestered into polyhedral protein bodies called carboxysomes.
37     The stable accumulation of proteins in a protein body compartment instead of vacuolar accumulatio
38 that gamma-zeins are essential for restoring protein body density and starch grain interaction in QPM
39 rm formation through a variety of effects on protein body density, size, and morphology.
40 evel during the period of zein synthesis and protein body development and declines to a low level at
41                              However, mutant protein bodies ectopically accumulate 22-kD alpha-zeins
42 is associated with small, irregularly shaped protein bodies, elevated levels of a 70-kDa chaperone in
43 e cytoplasm, and are distributed to both the protein body endoplasmic reticulum (ER) and cisternal ER
44 amine' class) are localized to the spherical protein body ER (PB-ER) in developing maize endosperm.
45 the cortical endoplasmic reticulum (ER), the protein body ER and the cisternal ER, in developing rice
46 dition of glutelin 3' untranslated region to protein body ER cis sequences, however, redirects RNA lo
47 artially redundant cis elements required for protein body ER targeting.
48         When isolated from the cisternal and protein body ER, the PDI protein resolves into a fast an
49  increase of binding protein (BiP) is in the protein body ER.
50 ts localization from the cisternal ER to the protein body ER.
51 zed protein, but instead are targeted to the protein body-ER (PB-ER) by a regulated process requiring
52 odes required for restricted localization to protein body-ER have previously been identified.
53 r gamma-zein family members function more in protein body expansion and not in protein body initiatio
54 D alpha-zein subfamilies severely restricted protein body expansion but did not induce morphological
55 otein body initiation but is not involved in protein body filling.
56 t that gamma-zein plays an important role in protein body formation and demonstrate the utility of to
57 sis of gamma-zeins could initiate and target protein body formation at specific regions of the rough
58 ese studies suggest that FL1 participates in protein body formation by facilitating the localization
59 asibility of using Zera technology to induce protein body formation in non-seed tissues.
60 double null mutant had negligible effects on protein body formation, the betaRNAi and gammaRNAi alone
61 n of the specific roles of family members in protein body formation.
62                        We suggest that other protein bodies formed in starvation conditions have a si
63 d beta-zein RNAis were stacked, resulting in protein bodies forming as honeycomb-like structures.
64 regulated in the fl2 mutant, specifically in protein body fractions where the mutation has its greate
65                                              Protein bodies from normal cultivars, such as P721N stud
66 n microscopy micrographs revealed that these protein bodies had a unique microstructure related to hi
67                                         Zein protein bodies in fl1 mutants are of normal size, shape,
68 olamine RNAs to the surface of the prolamine protein bodies in living endosperm cells, we adapted a t
69                          Prolamin-containing protein bodies in maize endosperm are composed of four d
70                                         Zein protein bodies in Mc endosperm are misshapen and are ass
71 PP1 was immunolocalized in slime plugs and P-protein bodies in sieve elements of the phloem.
72 nd Oh545o2 by increasing the surface area of protein bodies in the endosperm and creating a more exte
73 n these proteins leading to the formation of protein bodies in the endosperm.
74 storage proteins that form accretions called protein bodies in the rough endoplasmic reticulum of mai
75 1 complex was bound to promyelocyte leukemia protein bodies in undamaged cells.
76 t the 27-kilodalton (kD) gamma-zein controls protein body initiation but is not involved in protein b
77 on more in protein body expansion and not in protein body initiation.
78  (Zea mays), accumulate in accretions called protein bodies inside the endoplasmic reticulum (ER) of
79 Aux/IAAs into proteolytically active nuclear protein bodies, into which components of the SCF(TIR1),
80    Furthermore, consistent with the vacuolar/protein body location and glycoprotein character of thes
81 nts was explained collectively by C-reactive protein, body mass index, and high-density lipoprotein c
82 glycated hemoglobin A1c, level of C-reactive protein, body mass index, and platelet count were used t
83 ty lipoprotein, glucose, insulin, C-reactive protein, body mass index, and systolic and diastolic blo
84 erides, type 2 diabetes mellitus, C-reactive protein, body mass index, systolic blood pressure, and t
85 erides, type 2 diabetes mellitus, C-reactive protein, body mass index, systolic blood pressure, and t
86 e cloning of Fl1, which encodes a novel zein protein body membrane protein with three predicted trans
87 fl2 mutant exhibited increased PI content in protein body membranes at 18 d after pollination and mor
88                     By remaining anchored to protein body membranes during endosperm maturation, the
89 crease in storage protein synthesis, altered protein body morphology, and the synthesis of a novel 24
90 onstrain storage protein packing and perturb protein body morphology.
91 zein classes resulted in severe reduction in protein body number but normal protein body size and mor
92                                              Protein body number was reduced by over 90%, while prote
93 ddition to the increased surface area of the protein bodies of the highly digestible cultivar appear
94 ation of alpha- and beta-kafirins within the protein bodies of the highly digestible genotype were si
95  and stored in specialized organelles called protein bodies (PB).
96 rs to be linked to the improper formation of protein bodies (PBs) where zein storage proteins are dep
97 ized to the surface of the prolamine storage protein bodies (PBs), organelles bounded by the endoplas
98 s at the base of the folds instead of at the protein body periphery, as is typical of normal cultivar
99 entral hydrophobic core and the cross-linked protein body periphery, respectively, but little is know
100 ry arthropods such as extrafloral nectar and protein bodies provide indirect plant defence by attract
101 e found primarily associated with ER-derived protein bodies regardless of the presence of an ER stres
102 e 27-kD gamma-zein proteins on cisternal and protein body rough endoplasmic reticulum membranes.
103 ins is necessary for maintenance of a normal protein body shape.
104 ocated at the surface of prolamin-containing protein bodies, similar to other gamma-zeins.
105  reduction in protein body number but normal protein body size and morphology.
106 n body number was reduced by over 90%, while protein body size is similar to the wild type.
107                             Abnormalities in protein body structure and their interaction with starch
108 tly to the subnuclear promyelocytic leukemia protein bodies, suggesting that this protein may be invo
109                          Also, the number of protein bodies was increased in the aap1 endosperm, sugg
110                                              Protein bodies were also found in protein storage vacuol
111 es within cells, such as starch granules and protein bodies, were clearly identified.
112 gglomerates similar in structure to native P-protein bodies when transiently coexpressed in Nicotiana
113   Prolamines are retained in the ER lumen as protein bodies whereas glutelins are transported and sto

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